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Crystal structure of RTT109

Analyse Crystal structure of RTT109 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RIM
Type: protein
Length: 374 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Regulator of TY1 transposition protein 109
UniProt: Q07794
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Regulator of TY1 transposition protein 109	protein	374	32% helix, 24% strand	Q07794

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	375	0.68	0.81	49	empty
2	173	0.65	0.85	26	empty
3	102	0.40	0.76	17	empty
4	84	0.35	0.75	16	empty
5	66	0.31	0.75	14	empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

2RIM · Crystal structure of Rtt109 · the same entry in another collection · chain A against A, TM-score 1.00
Q07794 · AlphaFold monomer V2.0 prediction for histone acetyltransferase RTT109 (Q07794) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q07794
Elsewhere: RCSB PDB 2RIM · PDBe 2RIM · UniProt Q07794

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